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ribosomal S6 kinase 2 (ribosomal protein S6 kinase alpha 3, S6K-alpha 3, RPS6KA3, 90 kDa ribosomal protein S6 kinase 3, p90-RSK 3, RSK-2, pp90RSK2, insulin-stimulated protein kinase 1, ISPK-1)

Function: - serine/threonine kinase - may play a role in mediating the growth-factor & stress induced activation of the transcription factor CREB - forms a complex with either ERK1 or ERK2 in quiescent cells, transiently dissociates following mitogenic stimulation - activated by multiple phosphorylations on Thr & Ser (putative) - autophosphorylated on Ser-386, as part of the activation process (putative) - Ser-227 phosphorylation promotes Ser-386 phosphorylation & leads to basal activation - full activation by growth factors requires additional phosphorylation on Ser-369 (putative) Cofactor: Mg+2 (putative) Structure: - belongs to the protein kinase superfamily, AGC Ser/Thr protein kinase family, S6 kinase subfamily - contains 1 AGC-kinase C-terminal domain - contains 2 protein kinase domains Expression: - expressed in many tissues - highest levels in skeletal muscle Pathology: - defects in RPS6KA3 are the cause of Coffin-Lowry syndrome

Interactions

molecular events

General

ribosomal protein S6 kinase

Properties

SIZE: entity length = 740 aa MW = 84 kD COMPARTMENT: cytoplasm STATE: active state MOTIF: kinase domain SITE: 68-327 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 74-82 ATP-binding site NAME: ATP-binding site SITE: 100-100 aspartate residue {D193} Ser phosphorylation site {S227} Thr phosphorylation site {T231} AGC-kinase C-terminal {328-397} MOTIF: Thr phosphorylation site {T365} Ser phosphorylation site {S369} Ser phosphorylation site {S386} kinase domain SITE: 422-679 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 428-436 ATP-binding site NAME: ATP-binding site SITE: 451-451 aspartate residue {D539} Thr phosphorylation site {T577} Ser phosphorylation site {S715} Ser phosphorylation site {S737} MISC-INFO: RECOGNITION-MOTIF :SEQUENCE XRXX[S*]X :REF " - Kemp BE, Pearson RB. Protein kinase recognition sequence motifs. Trends Biochem Sci. 1990 Sep;15(9):342-6. Review. PMID: 2238044"

Database Correlations

OMIM correlations MORBIDMAP 300075 UniProt P51812 PFAM correlations Kegg hsa:6197 ENZYME 2.7.11.1

References

  1. UniProt :accession P51812
  2. Denton RM. Insulin signalling: search for the missing links. Nature. 1990 Nov 22;348(6299):286-7. PMID: 2250701
  3. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=RPS6KA3